Enzymes Topic 3.6 & 7.6 SPEED UP CHEMICAL REACTIONS!!!!!!!
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1 Enzymes Topic 3.6 & 7.6 SPEED UP CHEMICAL REACTIONS!!!!!!!
2 Key Words Enzyme Substrate Product Active Site Catalyst Activation Energy Denature Enzyme-Substrate Complex Lock & Key model Induced fit model Allosteric site
3 ENZYMES! Enzymes are protein molecules and catalysts They speed chemical reactions that occur in living organisms without being consumed Without enzymes, many of the reactions that occur within our bodies would not be able to happen fast enough to sustain life.
4 Characteristics of Enzymes In enzymatic reactions, the molecules at the beginning of the process that interact with the enzyme are called substrates. The enzyme converts them into different molecules, called the products Enzymes are very specific due to their 3D tertiary and quaternary structure ie) Catalase breaks up hydrogen peroxide into hydrogen and oxygen
5 What s in a name? The names of enzymes usually end in -ase» the enzyme in our saliva is called AMYLASE AMYLASE in our saliva breaks starch into maltose in order to simplify digestion.
6 Enzyme Specificity Enzymes are specific for one particular reaction or group of related reactions. ose = sugar Lactose Triglycerides Amylose ase = enzyme Protein (milk sugar) (lipid) (starch) Lactase Lipase Amylase Protease
7 Enzyme Action & Sucrase Enzyme sucrase breaks down a molecule of sucrose into glucose and fructose
8 How do Enzymes work?
9
10 Lock & Key Model A perfect match between the shape of the active site of an enzyme and the shape of its substrate like a perfect match between a lock and a key
11 So what s the problem? The lock-and key hypothesis cannot account for the binding and simultaneous change that is seen in many enzyme reactions, nor the fact that some enzymes can bind to more than one similarly shaped substrate. So alter the model.
12 Induced Fit Model The substrate causes or induces a slight change in the shape of the active site so it can fit perfectly. As the enzyme changes shape, the substrate molecule is activated so that it can react and the resulting product or products are released.
13 What is the difference?
14 How does an enzyme affect activation energy? Activation energy the amount of energy needed to trigger the reaction Metabolic reactions that occur in living organisms have to occur at the body temperature of the organism, which is never high enough to bring substrates to their transition state. Enzymes catalyze this process by providing a reaction pathway which is lower in the amount of energy required to activate the reaction. They reduce the activation energy required. Enzymes do not change the amount of products made, but only change the rate at which they are produced.
15 Activation Energy
16 Activation Energy The amount of activation energy that is required is considerably less when enzyme is present
17 Factors Affecting Enzymes Temperature Substrate concentration ph Enzyme concentration Heavy Metal Ions
18 Temperature Enzymes and their substrates meet as a result of random collisions As temperature increases, molecules move faster and there are more molecular collisions, causing more enzyme-substrate complexes to form.
19 Temperature Every enzyme has an optimal temperature at which it works best! A typical human enzyme works best at approximately 37 o C. A heat-tolerant organism enzyme works best at approximately 76 o C.
20 Temperature At low temperatures, molecules move slower and the likelihood of collisions is reduced. At high temperatures, the bonds holding the protein together are disrupted and the enzyme denatures. This changes the shape of the active site and the substrate can no longer bind.
21 ph Enzymes also have an optimal ph at which they work best. The digestive enzyme PEPSIN works best in the acidic environment of the stomach, ph 2.
22 ph Changes in ph can disrupt bonds and 3D shape of the enzyme Enzyme is said to be denatured no longer a catalyst
23 Substrate Concentration As [substrate] increases, so does reaction rate More substrate means more frequent collisions with enzyme Reaction rate will plateau when all the active sites are filled with substrate
24 Enzyme Concentration As [enzyme] increases, so does reaction rate More enzymes means more frequent collisions with substrate Reaction rate will plateau when all the active sites are filled with substrate; substrate becomes the limiting factor
25 Heavy Metal Ions The presence of heavy-metal ions can permanently alter the tertiary structure of an enzyme. Heavy metals such as Ag +, Hg 2+, Pb 2+ have strong affinities for SH groups and replace the hydrogen atoms in these groups. As the SH group is part of the side chain of the amino acid cysteine, it is present in many enzymes, which may then be affected by heavy metals.
26 What happens when an enzyme fails? TAY-SACHS DISEASE Hexosaminidase is the enzyme necessary to break down the fats in the brain and blood Lack of Hexosaminidase results in build up of fats in the brain This disease is inherited genetically FABRY DISEASE α-galactosidase is an enzyme that works in lysosomes to break down proteins, fats, nucleic acids & sugars A defect in the gene prevents the enzyme from folding properly and it cannot carry out its usual function The build up of Gb3 (its main substrate) causes damage to tissues and organs
27 Production of Lactose-Free Milk Lactose glucose + galactose Around 90% of all humans show some kind of lactose intolerance. People who are lactose intolerant can drink milk if it is lactose free. Symptoms of lactose intolerance include cramping, bloating, gas and diarrhoea Lactase is an enzyme extracted form a yeast that can digest the lactose to glucose and galactose. Lactose-free milk can be produced by passing milk over an enzyme bound to an inert carrier. Once the lactose molecule is broken down there are no lactose ill-effects.
28 Other reasons to produce lactose free products: Milk that has been broken down takes sweeter so manufacturers need to add less sugar to products such as yogurt. Fermentation rates are increased in lactose-free milk, so production rates increase Glucose is more soluble than lactose so smoother textures are produced
29
30 Enzyme Inhibition Inhibitors are molecules that can reduce or prevent enzyme action. TWO TYPES: 1) Competitive 2) Non-competitive
31 Competitive Inhibition Blocks the active site by binding to it, thereby preventing the substrate from binding. This slows enzyme activity. Adding more substrate will reduce the effect of the inhibitor. Ex: many drugs, penicillin, protease inhibitors used in HIV treatment
32 Non-competitive Inhibition The inhibitor binds to a place on the enzyme that is NOT the active site called the allosteric site. This changes the conformation of the enzyme (the substrate may no longer fit) and reduces its ability to catalyze the reaction (either slows it down or prevents it).
33 Competitive & Non-Competitive Inhibition
34 Metabolic Pathways & End Product Inhibition How metabolic pathways work: Chemical changes in living things often occurring with a number of intermediate stages or reactions. The processes are too big to happen in one step, so they are a series of little steps Each reaction is catalyzed by its own enzyme. Catabolic pathways breakdown molecules Anabolic pathways build up molecules
35 End Product Inhibition End product inhibition is negative feedback used to regulate the production of a given molecule. The end product of the pathway feeds back and becomes an allosteric inhibitor of the 1 st enzyme This stops the reaction so there will not be an excess production of the end product.
36
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